Most of the mechanical properties of living cells originate in the cytoskeleton, a dynamic network composed of crosslinked biopolymers, which gives the cell its shape and rigidity [1]}. One reason for its dynamic nature is that many of the crosslinking proteins, for example \(\alpha \) -actinin, form transient bonds with both finite binding and unbinding rates [2]}. Such crosslinking proteins, denoted as transient crosslinkers, introduce a distinct type of stress relaxation in semiflexible polymer networks, since the unbinding of crosslinkers allows the networks to flow at long time [3]}, [4]}, [5]}, [6]}, [7]}, [8]}. Previous theory and experiments involving reconstituted biopolymer networks have revealed a characteristic scaling exponent of \(\beta =1/2\)  for the frequency-dependent linear shear modulus [6]}, [7]}, [8]}. Unlike the Rouse model, in which the same exponent appears in the high-frequency regime [12]}, [13]}, [14]}, transient networks only exhibit the \(1/2\)  exponent in the low-frequency regime, indicating a different mechanism of stress relaxation from the Rouse model. Moreover, the Rouse model applies to flexible polymers, while the analogous high-frequency regime for semiflexible polymers such as actin is known theoretically and experimentally to exhibit a \(3/4\)  exponent [15]}, [16]}, [17]}, [18]}, [19]}, [20]}, [21]}.
